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PURIFICATION AND PROPERTIES OF BRAIN ALKALINE PHOSPHATASE

Authors

  • D. Thambi Dorai,

    1. Neurochemistry Laboratory, Department of Neurological Sciences, Christian Medical College Hospital, Vellore-632004, India
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  • B. K. Bachhawat

    1. Neurochemistry Laboratory, Department of Neurological Sciences, Christian Medical College Hospital, Vellore-632004, India
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    • 1

      Indian Institute of Experimental Medicine, Calcutta-700032, India.


Abstract

Abstract— Alkaline phosphatase from sheep brain has been purified to homogeneity. The method includes butanol extraction, fractional ethanol precipitation, ion-exchange chromatography on DEAE-cellulose, and on DEAE-Sephadex followed by Sephadex G-200 filtration. By these steps, the enzyme is purified 22,920-fold with 15% recovery. The homogeneous enzyme is shown to be a sialoglycoprotein in nature. Neuraminidase treatment reduces the electrophoretic mobility of the enzyme. The enzyme shows pyridoxal phosphate phosphatase activity along with p-nitrophenylphosphate phosphatase activity. Both these compounds behave as mutual alternate competitive substrates. The general properties of the enzyme are described.

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